COBQ_BACFN
ID COBQ_BACFN Reviewed; 495 AA.
AC Q5LCE1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=BF2524;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC and one molecule of ATP is hydrogenolyzed for each amidation.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; CR626927; CAH08224.1; -; Genomic_DNA.
DR RefSeq; WP_005787973.1; NC_003228.3.
DR AlphaFoldDB; Q5LCE1; -.
DR SMR; Q5LCE1; -.
DR STRING; 272559.BF9343_2443; -.
DR EnsemblBacteria; CAH08224; CAH08224; BF9343_2443.
DR KEGG; bfs:BF9343_2443; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_10; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000006731; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT CHAIN 1..495
FT /note="Cobyric acid synthase"
FT /id="PRO_1000002346"
FT DOMAIN 256..444
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 337
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 55071 MW; A13CC2733DE7082C CRC64;
MNKNLHPLML AGTGSDVGKS IIAAAFCRIF LQDGYHPAPF KAQNMALNSY ATPEGLEIGR
AQAVQAEAAG VPCHTDMNPL LLKPSSDHTS QVVLNGRPIG NRNAYEYFRR EGREELRKEV
HAAFDRLAAR YNPVVMEGAG SISEINLRDS DLVNLPMAMH AGADVILVAD IDRGGVFASV
YGSVMLLRPE ERKHIKGILI NKFRGDIRLF ESGVKMLEDL CGVPVVGVVP YYKDIYIEEE
DSVMLQTKNI RAGQGKVNVA VVLLRHLSNF TDFNVLERDP RVHLFYTNNT DELMKADIIL
LPGSKSTLSD LYELRRNGVA QAIVRAHREG ATVMGICGGY QLMGREVCDP DHVEGEIERL
PGLGLLPVST RMQGEKVTRQ VRFRFLEDSA VCEGYEIHMG TTTPLADVPV SPLNHLADGR
EDGYFVDRTC MGTYVHGILD NPSVIDYLLE PFADKLKETA FDYKAFKEEQ YDKLAAHVRK
HVDLPLIYQI LTDND